Inhibition of beta-amyloid aggregation by fluorescent dye labels

Mariana Amaro, Thorben Wellbrock, David Birch, Olaf Rolinski

Research output: Contribution to journalLetter

6 Citations (Scopus)
99 Downloads (Pure)

Abstract

The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.
Original languageEnglish
Article number063704
Number of pages5
JournalApplied Physics Letters
Volume104
Issue number6
Early online date12 Feb 2014
DOIs
Publication statusPublished - 12 Feb 2014

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dyes
fluorescence
tyrosine
oligomers
peptides
monomers
probes
decay

Keywords

  • aggregation
  • fluorescent dye labels
  • peptides

Cite this

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title = "Inhibition of beta-amyloid aggregation by fluorescent dye labels",
abstract = "The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.",
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Inhibition of beta-amyloid aggregation by fluorescent dye labels. / Amaro, Mariana; Wellbrock, Thorben; Birch, David; Rolinski, Olaf.

In: Applied Physics Letters, Vol. 104, No. 6, 063704, 12.02.2014.

Research output: Contribution to journalLetter

TY - JOUR

T1 - Inhibition of beta-amyloid aggregation by fluorescent dye labels

AU - Amaro, Mariana

AU - Wellbrock, Thorben

AU - Birch, David

AU - Rolinski, Olaf

PY - 2014/2/12

Y1 - 2014/2/12

N2 - The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.

AB - The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.

KW - aggregation

KW - fluorescent dye labels

KW - peptides

U2 - 10.1063/1.4865197

DO - 10.1063/1.4865197

M3 - Letter

VL - 104

JO - Applied Physics Letters

JF - Applied Physics Letters

SN - 0003-6951

IS - 6

M1 - 063704

ER -